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Database: UniProt
Entry: V4RH61_9CAUL
LinkDB: V4RH61_9CAUL
Original site: V4RH61_9CAUL 
ID   V4RH61_9CAUL            Unreviewed;       749 AA.
AC   V4RH61;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Transglycosylase SLT domain-containing protein {ECO:0000259|Pfam:PF01464};
GN   ORFNames=ABENE_11905 {ECO:0000313|EMBL:ESQ90668.1};
OS   Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ90668.1, ECO:0000313|Proteomes:UP000017837};
RN   [1] {ECO:0000313|EMBL:ESQ90668.1, ECO:0000313|Proteomes:UP000017837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ90668.1,
RC   ECO:0000313|Proteomes:UP000017837};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
CC   -!- SIMILARITY: Belongs to the virb1 family.
CC       {ECO:0000256|ARBA:ARBA00009387}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESQ90668.1}.
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DR   EMBL; AWGB01000022; ESQ90668.1; -; Genomic_DNA.
DR   RefSeq; WP_018079955.1; NZ_AWGB01000022.1.
DR   AlphaFoldDB; V4RH61; -.
DR   STRING; 1121022.GCA_000376105_00276; -.
DR   PATRIC; fig|1121022.4.peg.2414; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0741; Bacteria.
DR   Proteomes; UP000017837; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.20.10; Bacterial muramidases; 2.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 2.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017837};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..749
FT                   /note="Transglycosylase SLT domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004726574"
FT   DOMAIN          577..685
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          25..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   749 AA;  79645 MW;  C78DAA157D0C800D CRC64;
     MKPTHRALIS LSALGFALMA ATPGWTATSK TEKPTTEIRT AKPAEKKTDA KKAASKTSSK
     KTEVAEKSSK ASKKTAAGES DDAKPLKTKG KTANGKEKAK IADAAPEKGS KTSKASEKAS
     KKATGKSKSE LAEAKSSKKS KSELADALSG KTSGKKNSKK TEVAAAAPAK KSSKTAVKVA
     TVKAPAVVAT ITAPKVDAPV VMNAMPLPYG LVAGQGTPIT PVALNTPLSP YDTALYQSAF
     TLIDKGDYAG ADAQLAQVTD KRLMGYAQYN KLFSRGYNST YEELMAWLAD YGDQPMAMKV
     WGLAKRKKPE GAPDPAFPLL AGKPVLTGGN AIQLDGGTTL SGSTPVARAD ASAPASDTDL
     TPKSARSAYN NGQLAEAVRL GRKIGDHWVA GLASWRLKRY EDAMAEFTFV SSDPSTNAWT
     QSSGAYWAGR CAAKLGQKEQ ADTYFQLAAS FPFTFYGLLA EARLGVTPAI ALAQKGLPPT
     FSRDQRTALA ASLTSDFSWT HTNARAQRLN ALVQVGQHSE AQYELKTAIQ NSSNNDERQK
     WLALGAKTHL PVNQLTMTDR LFDVSLYPMP DIAPKGGYTV DKALIYALAR KESKFDASAH
     SYSGAYGLLQ LMPSTAALVE NDPSYNSKPK QLLTPSVNLR VGQNYIMRLK DSNIVDGDLL
     RTIAAYNAGP RPVKDAVSSL GNDADSLLVM ESIPVAQTRQ YVEEVAANYW IYRQIMGKTS
     KTLAAAAADA QIIDLTADSP AQAVAFADK
//
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